ID   GH109_SHEB8             Reviewed;         459 AA.
AC   A6WQ58;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Glycosyl hydrolase family 109 protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Shew185_2813;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Glycosidase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Note=Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
CC       {ECO:0000250};
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000753; ABS08947.1; -; Genomic_DNA.
DR   RefSeq; WP_012089617.1; NC_009665.1.
DR   AlphaFoldDB; A6WQ58; -.
DR   SMR; A6WQ58; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   KEGG; sbm:Shew185_2813; -.
DR   HOGENOM; CLU_046965_0_0_6; -.
DR   OMA; MESGKHA; -.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Signal.
FT   SIGNAL          1..31
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           32..459
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_5000260970"
FT   BINDING         64..65
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  51910 MW;  786AAF8C3CBDFB88 CRC64;
     MHNIHRRNFL KAAGAATAGL VTANIALSAY ASSVAPKPQA GKSVIGLIAP KMDVVRVGFI
     GVGERGFSHV EQFCHLEGVE LKAICDTHQA VLDRAVDHIV KQNRPKPAVY TGNDLSYRDL
     LSRDDIDIVI ISTPWEWHAP MAIETMESGK HAFVEVPMAL TVEECWQVVD TAERTQKNCM
     MMENVNYGRE ELMVLNMVRQ GVFGELLHGE AAYIHELRWQ MKEIDHKTGS WRTYWHTKRN
     GNLYPTHGLG PVSQYMNINR GDRFDYLTSM SSPALGRALY AKREFPADHE RNQLKYINGD
     INTSLIKTVK GRTIMVQHDT TTPRPYSRHN LIQGTNGVFA GFPNRIAVEN GGFGQSYHEW
     DMDMQKWYDK YDHPLWQRIG KEAEINGGHG GMDFVMLWRM IYCLRNGETL DQDVYDGASW
     SVVNILSEHS LNDRSNSVTF PDFTRGAWQT AKPLGIIGA